ID   HDEB_ECOL6              Reviewed;         108 AA.
AC   P0AET3; P26605;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Acid stress chaperone HdeB {ECO:0000255|HAMAP-Rule:MF_00947};
DE   Flags: Precursor;
GN   Name=hdeB {ECO:0000255|HAMAP-Rule:MF_00947}; OrderedLocusNames=c4320;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Required for optimal acid stress protection, which is
CC       important for survival of enteric bacteria in the acidic environment of
CC       the host stomach. Exhibits a chaperone-like activity at acidic pH by
CC       preventing the aggregation of many different periplasmic proteins.
CC       {ECO:0000255|HAMAP-Rule:MF_00947}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00947}.
CC   -!- SIMILARITY: Belongs to the HdeB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00947}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN82756.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN82756.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001298717.1; NC_004431.1.
DR   AlphaFoldDB; P0AET3; -.
DR   SMR; P0AET3; -.
DR   STRING; 199310.c4320; -.
DR   EnsemblBacteria; AAN82756; AAN82756; c4320.
DR   GeneID; 58463707; -.
DR   KEGG; ecc:c4320; -.
DR   eggNOG; ENOG50334GK; Bacteria.
DR   HOGENOM; CLU_149189_1_0_6; -.
DR   OMA; VAFWMLN; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:1990451; P:cellular stress response to acidic pH; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.890.10; -; 1.
DR   HAMAP; MF_00947; HdeB; 1.
DR   InterPro; IPR038303; HdeA/HdeB_sf.
DR   InterPro; IPR028623; HdeB.
DR   InterPro; IPR010486; HNS-dep_expression_A/B.
DR   Pfam; PF06411; HdeA; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chaperone; Periplasm; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00947"
FT   CHAIN           30..108
FT                   /note="Acid stress chaperone HdeB"
FT                   /id="PRO_0000045102"
FT   MOD_RES         93
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   108 AA;  12043 MW;  4E80163ACFD1399F CRC64;
     MNISSLRKAF IFMGAVAALS LVNAQSALAA NESAKDMTCQ EFIDLNPKAM TPVAWWMLHE
     ETVYKGGDTV TLNETDLTQI PKVIEYCKKN PQKNLYTFKN QASNDLPN